Several ongoing AAMP (angio-associated migratory cell protein) studies are being reported in the May 15th 1995 issue of Cancer Research. Published work completed last year includes the final sequencing results of AAMP's mRNA with the amino terminus, its tissue distribution and cell localization, specificity of anti-recombinant AAMP's reactivity to blotted human cell lysates tested with competing ligand (2.22 mg of recombinant AAMP generated for this purpose), a more accurate determination of AAMP's molecular weight (52 kDa), detection of a similar yeast protein, and additional heparin binding studies. New heparin binding studies with new ligand-receptor ratios generated more data points so that complete Scatchard and saturation curves with more information than previous ones were obtained. AAMP's amino terminus was obtained with the use of reverse transcriptase-PCR methodology and was identified on Southern blots with a nonradioactively labeled oligonucleotide probe. Immunoperoxidase studies with anti-recombinant AAMP using "antigen retrieval," via microwave treatment of tissue sections, showed strong staining for AAMP in endothelium, trophoblasts, poorly differentiated colon adenocarcinoma found in lymphatics, fibroblasts, some mononuclear inflammatory cells, cell surfaces of endometrial cells, and some neurons. Other data from this year not yet published include its experimental pI of 5.2 (nondenaturing conditions), its detection in the extracellular matrix of cultured endothelial cells, detection of immunoreactive species in serum, plasma, and the conditioned media of cultured melanoma cells, further characterization of its yeast homologue, YCRO72c, and the location of AAMP's gene on chromosome 2 in humans. A second publication on a rare type of thyroid carcinoma was also published. A third publication, "Growth factors and cytokines in tumor invasion and metastasis" is in press.